|
Name |
Accession |
Description |
Interval |
E-value |
| AtpD |
COG0055 |
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP ... |
1-463 |
0e+00 |
|
FoF1-type ATP synthase, beta subunit [Energy production and conversion]; FoF1-type ATP synthase, beta subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439825 [Multi-domain] Cd Length: 468 Bit Score: 990.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 1 MTKGRVTQLMGPVVDVRFEDGQLPAINNALVVRSKQsGEDLTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISV 80
Cdd:COG0055 3 MNTGKIVQVIGPVVDVEFPEGELPAIYNALEVENEG-GGELVLEVAQHLGDNTVRCIAMDSTDGLVRGMEVIDTGAPISV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 81 PVGDVTLGRVFNILGEKIDLDEPLPAGTRLdPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT 160
Cdd:COG0055 82 PVGEATLGRIFNVLGEPIDGKGPIEAKERR-PIHRPAPPFEEQSTKTEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 161 VLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQ 240
Cdd:COG0055 161 VLIMELIHNIAKEHGGVSVFAGVGERTREGNDLYREMKESGVLDKTALVFGQMNEPPGARLRVALTALTMAEYFRDEEGQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 241 DVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAPATTFAHL 320
Cdd:COG0055 241 DVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 321 DATTNLDRKLSEQGIYPAVDPLASTSRALDPEVVGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARR 400
Cdd:COG0055 321 DATTVLSRKIAELGIYPAVDPLDSTSRILDPLIVGEEHYRVAREVQRILQRYKELQDIIAILGMDELSEEDKLTVARARK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755605759 401 IQFFLSQNFHVAEQFTGQPGSYVPVKETVQGFKEILEGKYDDLPEDAFRLVGRIEEVVEKAKA 463
Cdd:COG0055 401 IQRFLSQPFFVAEQFTGIPGKYVPLEDTIRGFKEILDGEYDDLPEQAFYMVGTIDEAVEKAKK 463
|
|
| atpD |
TIGR01039 |
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are ... |
2-462 |
0e+00 |
|
ATP synthase, F1 beta subunit; The sequences of ATP synthase F1 alpha and beta subunits are related and both contain a nucleotide-binding site for ATP and ADP. They have a common amino terminal domain but vary at the C-terminus. The beta chain has catalytic activity, while the alpha chain is a regulatory subunit. Proton translocating ATP synthase, F1 beta subunit is homologous to proton translocating ATP synthase archaeal/vacuolar(V1), A subunit. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 211621 [Multi-domain] Cd Length: 461 Bit Score: 901.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 2 TKGRVTQLMGPVVDVRFEDGQLPAINNALVVRSKQSGeDLTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISVP 81
Cdd:TIGR01039 1 TKGKVVQVIGPVVDVEFEQGELPRIYNALKVQNRAES-ELTLEVAQHLGDDTVRTIAMGSTDGLVRGLEVIDTGAPISVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 82 VGDVTLGRVFNILGEKIDLDEPLPAGTRlDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTV 161
Cdd:TIGR01039 80 VGKETLGRIFNVLGEPIDEKGPIPAKER-WPIHRKAPSFEEQSTKVEILETGIKVIDLLAPYAKGGKIGLFGGAGVGKTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 162 LIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQD 241
Cdd:TIGR01039 159 LIQELINNIAKEHGGYSVFAGVGERTREGNDLYHEMKESGVIDKTALVYGQMNEPPGARMRVALTGLTMAEYFRDEQGQD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 242 VLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAPATTFAHLD 321
Cdd:TIGR01039 239 VLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGELQERITSTKTGSITSVQAVYVPADDLTDPAPATTFAHLD 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 322 ATTNLDRKLSEQGIYPAVDPLASTSRALDPEVVGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARRI 401
Cdd:TIGR01039 319 ATTVLSRKIAELGIYPAVDPLDSTSRLLDPSVVGEEHYDVARGVQQILQRYKELQDIIAILGMDELSEEDKLTVERARRI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755605759 402 QFFLSQNFHVAEQFTGQPGSYVPVKETVQGFKEILEGKYDDLPEDAFRLVGRIEEVVEKAK 462
Cdd:TIGR01039 399 QRFLSQPFFVAEVFTGQPGKYVPLKDTIRGFKEILEGKYDHLPEQAFYMVGTIEEVVEKAK 459
|
|
| atpB |
CHL00060 |
ATP synthase CF1 beta subunit |
3-465 |
0e+00 |
|
ATP synthase CF1 beta subunit
Pssm-ID: 214349 [Multi-domain] Cd Length: 494 Bit Score: 813.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 3 KGRVTQLMGPVVDVRFEDGQLPAINNALVVRSKQSGED---LTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPIS 79
Cdd:CHL00060 16 LGRITQIIGPVLDVAFPPGKMPNIYNALVVKGRDTAGQeinVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 80 VPVGDVTLGRVFNILGEKIDLDEPLPAGTRLdPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 159
Cdd:CHL00060 96 VPVGGATLGRIFNVLGEPVDNLGPVDTRTTS-PIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 160 TVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVI-------AKTAMVFGQMNEPPGARMRVALTGLTMAE 232
Cdd:CHL00060 175 TVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVIneqniaeSKVALVYGQMNEPPGARMRVGLTALTMAE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 233 YFRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPA 312
Cdd:CHL00060 255 YFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 313 PATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDPEVVGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDK 392
Cdd:CHL00060 335 PATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDR 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755605759 393 LVVSRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVQGFKEILEGKYDDLPEDAFRLVGRIEEVVEKAKASE 465
Cdd:CHL00060 415 LTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAANLE 487
|
|
| alt_F1F0_F1_bet |
TIGR03305 |
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic ... |
4-456 |
0e+00 |
|
alternate F1F0 ATPase, F1 subunit beta; A small number of taxonomically diverse prokaryotic species have what appears to be a second ATP synthase, in addition to the normal F1F0 ATPase in bacteria and A1A0 ATPase in archaea. These enzymes use ion gradients to synthesize ATP, and in principle may run in either direction. This model represents the F1 beta subunit of this apparent second ATP synthase.
Pssm-ID: 132348 [Multi-domain] Cd Length: 449 Bit Score: 584.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 4 GRVTQLMGPVVDVRFeDGQLPAINNalVVRSKQSGEdLTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISVPVG 83
Cdd:TIGR03305 1 GHVVAVRGSIVDVRF-DGELPAIHS--VLRAGREGE-VVVEVLSQLDAHHVRGIALTPTQGLARGMPVRDSGGPLKAPVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 84 DVTLGRVFNILGEKIDLDEPlPAGTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLI 163
Cdd:TIGR03305 77 KPTLSRMFDVFGNTIDRREP-PKDVEWRSVHQAPPTLTRRSSKSEVFETGIKAIDVLVPLERGGKAGLFGGAGVGKTVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 164 QELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDEQGQDVL 243
Cdd:TIGR03305 156 TEMIHNMVGQHQGVSIFCGIGERCREGEELYREMKEAGVLDNTVMVFGQMNEPPGARFRVGHTALTMAEYFRDDEKQDVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 244 LFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAPATTFAHLDAT 323
Cdd:TIGR03305 236 LLIDNIFRFIQAGSEVSGLLGQMPSRLGYQPTLGTELAELEERIATTSDGAITSIQAVYVPADDFTDPAAVHTFSHLSAS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 324 TNLDRKLSEQGIYPAVDPLASTSRALDPEVVGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARRIQF 403
Cdd:TIGR03305 316 LVLSRKRASEGLYPAIDPLQSTSKMATPGIVGERHYDLAREVRQTLAQYEELKDIIAMLGLEQLSREDRRVVNRARRLER 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 755605759 404 FLSQNFHVAEQFTGQPGSYVPVKETVQGFKEILEGKYDDLPEDAFRLVGRIEE 456
Cdd:TIGR03305 396 FLTQPFFTTEQFTGMKGKTVSLEDALDGCERILNDEFQDYPERDLYMIGKIDE 448
|
|
| F1-ATPase_beta_CD |
cd01133 |
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma ... |
79-351 |
0e+00 |
|
F1 ATP synthase beta subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410877 [Multi-domain] Cd Length: 277 Bit Score: 571.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 79 SVPVGDVTLGRVFNILGEKIDLDEPLPAGTRlDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 158
Cdd:cd01133 1 SVPVGEETLGRIFNVLGEPIDERGPIKAKER-WPIHREAPEFVELSTEQEILETGIKVVDLLAPYAKGGKIGLFGGAGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 159 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIA-----KTAMVFGQMNEPPGARMRVALTGLTMAEY 233
Cdd:cd01133 80 KTVLIMELINNIAKAHGGYSVFAGVGERTREGNDLYHEMKESGVINldglsKVALVYGQMNEPPGARARVALTGLTMAEY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 234 FRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAP 313
Cdd:cd01133 160 FRDEEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATEMGSLQERITSTKKGSITSVQAVYVPADDLTDPAP 239
|
250 260 270
....*....|....*....|....*....|....*...
gi 755605759 314 ATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDP 351
Cdd:cd01133 240 ATTFAHLDATTVLSRGIAELGIYPAVDPLDSTSRILDP 277
|
|
| RecA-like_ion-translocating_ATPases |
cd19476 |
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the ... |
79-348 |
3.88e-125 |
|
RecA-like domain of ion-translocating ATPases; RecA-like NTPases. This family includes the NTP-binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.
Pssm-ID: 410884 [Multi-domain] Cd Length: 270 Bit Score: 364.47 E-value: 3.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 79 SVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLdPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 158
Cdd:cd19476 1 SVPVGPELLGRILDGLGEPLDGLPPIKTKQRR-PIHLKAPNPIERLPPEEPLQTGIKVIDLLAPYGRGQKIGIFGGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 159 KTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQ 238
Cdd:cd19476 80 KTVLAMQLARNQAKAHAGVVVFAGIGERGREVNDLYEEFTKSGAMERTVVVANTANDPPGARMRVPYTGLTIAEYFRD-N 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 239 GQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITST--DKGSVTSIQAIYVPADDYTDPAPATT 316
Cdd:cd19476 159 GQHVLLIIDDISRYAEALREMSALLGEPPGREGYPPYLFTKLATLYERAGKVkdGGGSITAIPAVSTPGDDLTDPIPDNT 238
|
250 260 270
....*....|....*....|....*....|..
gi 755605759 317 FAHLDATTNLDRKLSEQGIYPAVDPLASTSRA 348
Cdd:cd19476 239 FAILDGQIVLSRELARKGIYPAINVLDSTSRV 270
|
|
| ATP-synt_ab |
pfam00006 |
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP ... |
133-346 |
1.70e-99 |
|
ATP synthase alpha/beta family, nucleotide-binding domain; This entry includes the ATP synthase alpha and beta subunits, the ATP synthase associated with flagella and the termination factor Rho.
Pssm-ID: 425417 [Multi-domain] Cd Length: 212 Bit Score: 296.96 E-value: 1.70e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 133 GIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQehgGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQ 212
Cdd:pfam00006 1 GIRAIDGLLPIGRGQRIGIFGGSGVGKTVLAGMIARQASA---DVVVYALIGERGREVREFIEELLGSGALKRTVVVVAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 213 MNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTD- 291
Cdd:pfam00006 78 SDEPPLARYRAPYTALTIAEYFRD-QGKDVLLIMDSLTRFAEALREISLALGEPPGREGYPPSVFSLLARLLERAGRVKg 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755605759 292 -KGSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTS 346
Cdd:pfam00006 157 kGGSITALPTVLVPGDDITDPIPDNTRSILDGQIVLSRDLAEKGHYPAIDVLASVS 212
|
|
| FliI |
COG1157 |
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular ... |
4-436 |
7.07e-70 |
|
Flagellar biosynthesis/type III secretory pathway ATPase FliI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 440771 [Multi-domain] Cd Length: 433 Bit Score: 228.38 E-value: 7.07e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 4 GRVTQLMGPVVDVRfedGQLPAINNALVVRSkQSGEDLTLEValhLGDHSVRTIAM--SSTDGFQRGAEVEDLGRPISVP 81
Cdd:COG1157 21 GRVTRVVGLLIEAV---GPDASIGELCEIET-ADGRPVLAEV---VGFRGDRVLLMplGDLEGISPGARVVPTGRPLSVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 82 VGDVTLGRVFNILGEKIDlDEPLPAGTRLDPIHREAPDFenLSTE--TEILETGIKVVDLLAPYIKGGKIGLFGGAGVGK 159
Cdd:COG1157 94 VGDGLLGRVLDGLGRPLD-GKGPLPGEERRPLDAPPPNP--LERAriTEPLDTGVRAIDGLLTVGRGQRIGIFAGSGVGK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 160 TVLIQELINNIAQEhggISVFAGVGERTRE-----GNDLYYE-MSDSGVIAKTAmvfgqmNEPPGARMRVALTGLTMAEY 233
Cdd:COG1157 171 STLLGMIARNTEAD---VNVIALIGERGREvrefiEDDLGEEgLARSVVVVATS------DEPPLMRLRAAYTATAIAEY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 234 FRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTsiqAIY---VPADDYTD 310
Cdd:COG1157 242 FRD-QGKNVLLLMDSLTRFAMAQREIGLAAGEPPATRGYPPSVFALLPRLLERAGNGGKGSIT---AFYtvlVEGDDMND 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 311 PAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDIIAI----LGMDE 386
Cdd:COG1157 318 PIADAVRGILDGHIVLSRKLAERGHYPAIDVLASISRVM-PDIVSPEHRALARRLRRLLARYEENEDLIRIgayqPGSDP 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 755605759 387 LSDEdklVVSRARRIQFFLSQNFHvaeqftgqpgSYVPVKETVQGFKEIL 436
Cdd:COG1157 397 ELDE---AIALIPAIEAFLRQGMD----------ERVSFEESLAQLAELL 433
|
|
| ATP-synt_F1_beta_C |
cd18110 |
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of ... |
353-460 |
3.38e-69 |
|
F1-ATP synthase beta (B) subunit, C-terminal domain; The beta (B) subunit of the F1 complex of F0F1-ATP synthase, C-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349745 [Multi-domain] Cd Length: 108 Bit Score: 215.42 E-value: 3.38e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 353 VVGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARRIQFFLSQNFHVAEQFTGQPGSYVPVKETVQGF 432
Cdd:cd18110 1 IVGEEHYDVARGVQKILQRYKELQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFFVAEVFTGSPGKYVPLKDTIKGF 80
|
90 100
....*....|....*....|....*...
gi 755605759 433 KEILEGKYDDLPEDAFRLVGRIEEVVEK 460
Cdd:cd18110 81 KEILDGEYDDLPEQAFYMVGTIDEAVEK 108
|
|
| ATPase_flagellum-secretory_path_III |
cd01136 |
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; ... |
79-347 |
9.92e-61 |
|
Flagellum-specific ATPase/type III secretory pathway virulence-related protein; Flagellum-specific ATPase/type III secretory pathway virulence-related protein. This group of ATPases are responsible for the export of flagellum and virulence-related proteins. The bacterial flagellar motor is similar to the F0F1-ATPase, in that they both are proton-driven rotary molecular devices. However, the main function of the bacterial flagellar motor is to rotate the flagellar filament for cell motility. Intracellular pathogens such as Salmonella and Chlamydia also have proteins which are similar to the flagellar-specific ATPase, but function in the secretion of virulence-related proteins via the type III secretory pathway.
Pssm-ID: 410880 [Multi-domain] Cd Length: 265 Bit Score: 199.32 E-value: 9.92e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 79 SVPVGDVTLGRVFNILGEKIDlDEPLPAGTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVG 158
Cdd:cd01136 1 SIPVGDGLLGRVIDALGEPLD-GKGLPDEPERRPLIAAPPNPLKRAPIEQPLPTGVRAIDGLLTCGEGQRIGIFAGSGVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 159 KTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQ 238
Cdd:cd01136 80 KSTLLGMIARNTDAD---VNVIALIGERGREVREFIEKDLGEEGLKRSVLVVATSDESPLLRVRAAYTATAIAEYFRD-Q 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 239 GQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAPATTFA 318
Cdd:cd01136 156 GKKVLLLMDSLTRFAMAQREVGLAAGEPPTRRGYPPSVFALLPRLLERAGNGEKGSITAFYTVLVEGDDFNDPIADEVRS 235
|
250 260
....*....|....*....|....*....
gi 755605759 319 HLDATTNLDRKLSEQGIYPAVDPLASTSR 347
Cdd:cd01136 236 ILDGHIVLSRRLAERGHYPAIDVLASISR 264
|
|
| PRK06820 |
PRK06820 |
EscN/YscN/HrcN family type III secretion system ATPase; |
8-408 |
1.14e-57 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180712 [Multi-domain] Cd Length: 440 Bit Score: 196.57 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 8 QLMGPVVDV--RFEDGQLPAINNALVVRSKQSGedLTLEVALHLGDHSVRTiAMSSTDGFQRGAEVEDLGRPISVPVGDV 85
Cdd:PRK06820 28 RYRGPIVEIgpTLLRASLPGVAQGELCRIEPQG--MLAEVVSIEQEMALLS-PFASSDGLRCGQWVTPLGHMHQVQVGAD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 86 TLGRVFNILGEKIDLDEPLpaGTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQE 165
Cdd:PRK06820 105 LAGRILDGLGAPIDGGPPL--TGQWRELDCPPPSPLTRQPIEQMLTTGIRAIDGILSCGEGQRIGIFAAAGVGKSTLLGM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 166 LINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLF 245
Cdd:PRK06820 183 LCADSAAD---VMVLALIGERGREVREFLEQVLTPEARARTVVVVATSDRPALERLKGLSTATTIAEYFRD-RGKKVLLM 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 246 IDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAPATTFAHLDATTN 325
Cdd:PRK06820 259 ADSLTRYARAAREIGLAAGEPPAAGSFPPSVFANLPRLLERTGNSDRGSITAFYTVLVEGDDMNEPVADEVRSLLDGHIV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 326 LDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDIIAI----LGMDELSDEdklVVSRARRI 401
Cdd:PRK06820 339 LSRRLAGAGHYPAIDIAASVSRIM-PQIVSAGQLAMAQKLRRMLACYQEIELLVRVgeyqAGEDLQADE---ALQRYPAI 414
|
....*..
gi 755605759 402 QFFLSQN 408
Cdd:PRK06820 415 CAFLQQD 421
|
|
| PRK06936 |
PRK06936 |
EscN/YscN/HrcN family type III secretion system ATPase; |
3-415 |
2.94e-52 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 180762 [Multi-domain] Cd Length: 439 Bit Score: 182.26 E-value: 2.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 3 KGRVTQLMGPVVD-----VRFedGQLPAINNAlvvrskqsGEDLTL--EVALHLGDHSVRTiAMSSTDGFQRGAEVEDLG 75
Cdd:PRK06936 24 RGRVTQVTGTILKavvpgVRI--GELCYLRNP--------DNSLSLqaEVIGFAQHQALLT-PLGEMYGISSNTEVSPTG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 76 RPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLdPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGA 155
Cdd:PRK06936 93 TMHQVGVGEHLLGRVLDGLGQPFDGGHPPEPAAWY-PVYADAPAPMSRRLIETPLSLGVRVIDGLLTCGEGQRMGIFAAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 156 GVGKTVLIQELINNIAQEhggISVFAGVGERTREGND-LYYEMSDSGvIAKTAMVFGQMNEPPGARMRVALTGLTMAEYF 234
Cdd:PRK06936 172 GGGKSTLLASLIRSAEVD---VTVLALIGERGREVREfIESDLGEEG-LRKAVLVVATSDRPSMERAKAGFVATSIAEYF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 235 RDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPADDYTDPAPA 314
Cdd:PRK06936 248 RD-QGKRVLLLMDSVTRFARAQREIGLAAGEPPTRRGYPPSVFAALPRLMERAGQSDKGSITALYTVLVEGDDMTEPVAD 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 315 TTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDpEVVGEEHYRVAVEVQQTLQKYRELQDIIAI----LGMDELSDE 390
Cdd:PRK06936 327 ETRSILDGHIILSRKLAAANHYPAIDVLRSASRVMN-QIVSKEHKTWAGRLRELLAKYEEVELLLQIgeyqKGQDKEADQ 405
|
410 420
....*....|....*....|....*
gi 755605759 391 dklVVSRARRIQFFLSQNFHVAEQF 415
Cdd:PRK06936 406 ---AIERIGAIRGFLRQGTHELSHF 427
|
|
| fliI |
PRK06002 |
flagellar protein export ATPase FliI; |
88-347 |
1.85e-51 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 235666 [Multi-domain] Cd Length: 450 Bit Score: 180.19 E-value: 1.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 88 GRVFNILGEKIDLDEPLPAGTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELi 167
Cdd:PRK06002 107 GRVINALGEPIDGLGPLAPGTRPMSIDATAPPAMTRARVETGLRTGVRVIDIFTPLCAGQRIGIFAGSGVGKSTLLAML- 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 168 nniAQEHGGISV-FAGVGERTREGNDLYYE-MSDSgvIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLF 245
Cdd:PRK06002 186 ---ARADAFDTVvIALVGERGREVREFLEDtLADN--LKKAVAVVATSDESPMMRRLAPLTATAIAEYFRD-RGENVLLI 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 246 IDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERI--TSTDKGSVTSIQAIYVPADDYTDPAPATTFAHLDAT 323
Cdd:PRK06002 260 VDSVTRFAHAAREVALAAGEPPVARGYPPSVFSELPRLLERAgpGAEGGGSITGIFSVLVDGDDHNDPVADSIRGTLDGH 339
|
250 260
....*....|....*....|....
gi 755605759 324 TNLDRKLSEQGIYPAVDPLASTSR 347
Cdd:PRK06002 340 IVLDRAIAEQGRYPAVDPLASISR 363
|
|
| fliI |
PRK07721 |
flagellar protein export ATPase FliI; |
68-381 |
7.99e-50 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181092 [Multi-domain] Cd Length: 438 Bit Score: 175.68 E-value: 7.99e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 68 GAEVEDLGRPISVPVGDVTLGRVFNILGEKIDlDEPLPAGTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGG 147
Cdd:PRK07721 81 GCLVEATGKPLEVKVGSGLIGQVLDALGEPLD-GSALPKGLAPVSTDQDPPNPLKRPPIREPMEVGVRAIDSLLTVGKGQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 148 KIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGND-LYYEMSDSGvIAKTAMVFGQMNEPPGARMRVALT 226
Cdd:PRK07721 160 RVGIFAGSGVGKSTLMGMIARNTSAD---LNVIALIGERGREVREfIERDLGPEG-LKRSIVVVATSDQPALMRIKGAYT 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 227 GLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQAIYVPAD 306
Cdd:PRK07721 236 ATAIAEYFRD-QGLNVMLMMDSVTRVAMAQREIGLAVGEPPTTKGYTPSVFAILPKLLERTGTNASGSITAFYTVLVDGD 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755605759 307 DYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDIIAI 381
Cdd:PRK07721 315 DMNEPIADTVRGILDGHFVLDRQLANKGQYPAINVLKSVSRVM-NHIVSPEHKEAANRFRELLSTYQNSEDLINI 388
|
|
| PRK08149 |
PRK08149 |
FliI/YscN family ATPase; |
49-379 |
1.21e-49 |
|
FliI/YscN family ATPase;
Pssm-ID: 236166 [Multi-domain] Cd Length: 428 Bit Score: 174.80 E-value: 1.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 49 LGDHSVRTI--AMSSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKID-LDEPLPAGTR--LDPIHREAPDFENL 123
Cdd:PRK08149 49 VGFQRERTIlsLIGNAQGLSRQVVLKPTGKPLSVWVGEALLGAVLDPTGKIVErFDAPPTVGPIseERVIDVAPPSYAER 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 124 STETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVI 203
Cdd:PRK08149 129 RPIREPLITGVRAIDGLLTCGVGQRMGIFASAGCGKTSLMNMLIEHSEAD---VFVIGLIGERGREVTEFVESLRASSRR 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 204 AKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRL 283
Cdd:PRK08149 206 EKCVLVYATSDFSSVDRCNAALVATTVAEYFRD-QGKRVVLFIDSMTRYARALRDVALAAGELPARRGYPASVFDSLPRL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 284 QERITSTDKGSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDpEVVGEEHYRVAV 363
Cdd:PRK08149 285 LERPGATLAGSITAFYTVLLESEEEPDPIGDEIRSILDGHIYLSRKLAAKGHYPAIDVLKSVSRVFG-QVTDPKHRQLAA 363
|
330
....*....|....*.
gi 755605759 364 EVQQTLQKYRELQDII 379
Cdd:PRK08149 364 AFRKLLTRLEELQLFI 379
|
|
| PRK09099 |
PRK09099 |
type III secretion system ATPase; Provisional |
60-407 |
9.47e-48 |
|
type III secretion system ATPase; Provisional
Pssm-ID: 169656 [Multi-domain] Cd Length: 441 Bit Score: 170.33 E-value: 9.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 60 SSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLpAGTRLDPIHREAPDFENLSTETEILETGIKVVDL 139
Cdd:PRK09099 78 GELGGLSRGTRVIGLGRPLSVPVGPALLGRVIDGLGEPIDGGGPL-DCDELVPVIAAPPDPMSRRMVEAPLPTGVRIVDG 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 140 LAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGA 219
Cdd:PRK09099 157 LMTLGEGQRMGIFAPAGVGKSTLMGMFARGTQCD---VNVIALIGERGREVREFIELILGEDGMARSVVVCATSDRSSIE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 220 RMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTSIQ 299
Cdd:PRK09099 234 RAKAAYVATAIAEYFRD-RGLRVLLMMDSLTRFARAQREIGLAAGEPPARRGFPPSVFAELPRLLERAGMGETGSITALY 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 300 AIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDII 379
Cdd:PRK09099 313 TVLAEDESGSDPIAEEVRGILDGHMILSREIAARNQYPAIDVLGSLSRVM-PQVVPREHVQAAGRLRQLLAKHREVETLL 391
|
330 340 350
....*....|....*....|....*....|..
gi 755605759 380 AI----LGMDELSDEdklVVSRARRIQFFLSQ 407
Cdd:PRK09099 392 QVgeyrAGSDPVADE---AIAKIDAIRDFLSQ 420
|
|
| fliI |
PRK08927 |
flagellar protein export ATPase FliI; |
1-381 |
9.59e-47 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 236351 [Multi-domain] Cd Length: 442 Bit Score: 167.46 E-value: 9.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 1 MTKGRVTQLMGPVVDVRfedGQLPAIN-NALVVRSKQSGEDLTLEValhLGDHSVRTIAM--SSTDGFQRGAEVEDLGRP 77
Cdd:PRK08927 16 VIYGRVVAVRGLLVEVA---GPIHALSvGARIVVETRGGRPVPCEV---VGFRGDRALLMpfGPLEGVRRGCRAVIANAA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 78 ISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGV 157
Cdd:PRK08927 90 AAVRPSRAWLGRVVNALGEPIDGKGPLPQGPVPYPLRAPPPPAHSRARVGEPLDLGVRALNTFLTCCRGQRMGIFAGSGV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 158 GKTVLIQELINNIAQEhggISVFAGVGERTRE-----GNDLYYE-MSDSGVIAKTAmvfgqmNEPPGARMRVALTGLTMA 231
Cdd:PRK08927 170 GKSVLLSMLARNADAD---VSVIGLIGERGREvqeflQDDLGPEgLARSVVVVATS------DEPALMRRQAAYLTLAIA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 232 EYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERI--TSTDKGSVTSIQAIYVPADDYT 309
Cdd:PRK08927 241 EYFRD-QGKDVLCLMDSVTRFAMAQREIGLSAGEPPTTKGYTPTVFAELPRLLERAgpGPIGEGTITGLFTVLVDGDDHN 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755605759 310 DPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDIIAI 381
Cdd:PRK08927 320 EPVADAVRGILDGHIVMERAIAERGRYPAINVLKSVSRTM-PGCNDPEENPLVRRARQLMATYADMEELIRL 390
|
|
| fliI |
PRK08472 |
flagellar protein export ATPase FliI; |
4-437 |
2.55e-46 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181439 [Multi-domain] Cd Length: 434 Bit Score: 166.01 E-value: 2.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 4 GRVTQLMGPVVDVRfedGQLPAINNALVVRSKQSGEDLTLEVALHLGDHSVRTiAMSSTDGFQRGAEVEDLGRPISVPVG 83
Cdd:PRK08472 20 GSITKISPTIIEAD---GLNPSVGDIVKIESSDNGKECLGMVVVIEKEQFGIS-PFSFIEGFKIGDKVFISKEGLNIPVG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 84 DVTLGRVFNILGEKIDLDEPLPAgTRLDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLI 163
Cdd:PRK08472 96 RNLLGRVVDPLGRPIDGKGAIDY-ERYAPIMKAPIAAMKRGLIDEVFSVGVKSIDGLLTCGKGQKLGIFAGSGVGKSTLM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 164 QELINN-IAQehggISVFAGVGERTRE---------GNDLyyemSDSGVIAKTAmvfgqmNEPPGARMRVALTGLTMAEY 233
Cdd:PRK08472 175 GMIVKGcLAP----IKVVALIGERGREipefieknlGGDL----ENTVIVVATS------DDSPLMRKYGAFCAMSVAEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 234 FRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTD-KGSVTSIQAIYVPADDYTDPA 312
Cdd:PRK08472 241 FKN-QGLDVLFIMDSVTRFAMAQREIGLALGEPPTSKGYPPSVLSLLPQLMERAGKEEgKGSITAFFTVLVEGDDMSDPI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 313 PATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDpEVVGEEHYRVAVEVQQTLQKYRELQDIIAI----LGMDELS 388
Cdd:PRK08472 320 ADQSRSILDGHIVLSRELTDFGIYPPINILNSASRVMN-DIISPEHKLAARKFKRLYSLLKENEVLIRIgayqKGNDKEL 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 755605759 389 DEdklVVSRARRIQFFLSQNFHvaEQFtgqpgsyvPVKETVQGFKEILE 437
Cdd:PRK08472 399 DE---AISKKEFMEQFLKQNPN--ELF--------PFEQTFEQLEEILR 434
|
|
| PRK07594 |
PRK07594 |
EscN/YscN/HrcN family type III secretion system ATPase; |
60-390 |
1.05e-45 |
|
EscN/YscN/HrcN family type III secretion system ATPase;
Pssm-ID: 136438 [Multi-domain] Cd Length: 433 Bit Score: 164.36 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 60 SSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDlDEPLPAGTRLDpihREAPDFENLSTE--TEILETGIKVV 137
Cdd:PRK07594 71 TSTIGLHCGQQVMALRRRHQVPVGEALLGRVIDGFGRPLD-GRELPDVCWKD---YDAMPPPAMVRQpiTQPLMTGIRAI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 138 DLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPP 217
Cdd:PRK07594 147 DSVATCGEGQRVGIFSAPGVGKSTLLAMLCNAPDAD---SNVLVLIGERGREVREFIDFTLSEETRKRCVIVVATSDRPA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 218 GARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKGSVTS 297
Cdd:PRK07594 224 LERVRALFVATTIAEFFRD-NGKRVVLLADSLTRYARAAREIALAAGETAVSGEYPPGVFSALPRLLERTGMGEKGSITA 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 298 IQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQD 377
Cdd:PRK07594 303 FYTVLVEGDDMNEPLADEVRSLLDGHIVLSRRLAERGHYPAIDVLATLSRVF-PVVTSHEHRQLAAILRRCLALYQEVEL 381
|
330
....*....|....*..
gi 755605759 378 IIAI----LGMDELSDE 390
Cdd:PRK07594 382 LIRIgeyqRGVDTDTDK 398
|
|
| fliI |
PRK05688 |
flagellar protein export ATPase FliI; |
61-407 |
3.18e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 168181 [Multi-domain] Cd Length: 451 Bit Score: 161.05 E-value: 3.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 61 STDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPA-------GTRLDPIHREAPDfenlstetEILETG 133
Cdd:PRK05688 84 SVAGIAPGARVVPLADTGRLPMGMSMLGRVLDGAGRALDGKGPMKAedwvpmdGPTINPLNRHPIS--------EPLDVG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 134 IKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQM 213
Cdd:PRK05688 156 IRSINGLLTVGRGQRLGLFAGTGVGKSVLLGMMTRFTEAD---IIVVGLIGERGREVKEFIEHILGEEGLKRSVVVASPA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 214 NEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDKG 293
Cdd:PRK05688 233 DDAPLMRLRAAMYCTRIAEYFRD-KGKNVLLLMDSLTRFAQAQREIALAIGEPPATKGYPPSVFAKLPKLVERAGNAEPG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 294 --SVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQK 371
Cdd:PRK05688 312 ggSITAFYTVLSEGDDQQDPIADSARGVLDGHIVLSRRLAEEGHYPAIDIEASISRVM-PQVVDPEHLRRAQRFKQLWSR 390
|
330 340 350
....*....|....*....|....*....|....*..
gi 755605759 372 YRELQDIIAILGMDELSD-EDKLVVSRARRIQFFLSQ 407
Cdd:PRK05688 391 YQQSRDLISVGAYVAGGDpETDLAIARFPHLVQFLRQ 427
|
|
| fliI |
PRK08972 |
flagellar protein export ATPase FliI; |
68-381 |
3.71e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 181599 [Multi-domain] Cd Length: 444 Bit Score: 160.64 E-value: 3.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 68 GAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLdpiHREAPDFENLSTE--TEILETGIKVVDLLAPYIK 145
Cdd:PRK08972 85 GARVTPLGEQSGLPVGMSLLGRVIDGVGNPLDGLGPIYTDQRA---SRHSPPINPLSRRpiTEPLDVGVRAINAMLTVGK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 146 GGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVAL 225
Cdd:PRK08972 162 GQRMGLFAGSGVGKSVLLGMMTRGTTAD---VIVVGLVGERGREVKEFIEEILGEEGRARSVVVAAPADTSPLMRLKGCE 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 226 TGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERI--TSTDKGSVTSIQAIYV 303
Cdd:PRK08972 239 TATTIAEYFRD-QGLNVLLLMDSLTRYAQAQREIALAVGEPPATKGYPPSVFAKLPALVERAgnGGPGQGSITAFYTVLT 317
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755605759 304 PADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDIIAI 381
Cdd:PRK08972 318 EGDDLQDPIADASRAILDGHIVLSRELADSGHYPAIDIEASISRVM-PMVISEEHLEAMRRVKQVYSLYQQNRDLISI 394
|
|
| fliI |
PRK06793 |
flagellar protein export ATPase FliI; |
62-407 |
7.26e-44 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180696 [Multi-domain] Cd Length: 432 Bit Score: 159.37 E-value: 7.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 62 TDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKidLDEPlPAGTRLDPIHREAPDFENLSTE--TEILETGIKVVDL 139
Cdd:PRK06793 73 TEKVCYGDSVTLIAEDVVIPRGNHLLGKVLSANGEV--LNEE-AENIPLQKIKLDAPPIHAFEREeiTDVFETGIKSIDS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 140 LAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGND-LYYEMSDSGvIAKTAMVFGQMNEPPG 218
Cdd:PRK06793 150 MLTIGIGQKIGIFAGSGVGKSTLLGMIAKNAKAD---INVISLVGERGREVKDfIRKELGEEG-MRKSVVVVATSDESHL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 219 ARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAvGYQPTLATEMGRLQERITSTDKGSVTSI 298
Cdd:PRK06793 226 MQLRAAKLATSIAEYFRD-QGNNVLLMMDSVTRFADARRSVDIAVKELPIG-GKTLLMESYMKKLLERSGKTQKGSITGI 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 299 QAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDpEVVGEEHYRVAVEVQQTLQKYRElQDI 378
Cdd:PRK06793 304 YTVLVDGDDLNGPVPDLARGILDGHIVLKRELATLSHYPAISVLDSVSRIME-EIVSPNHWQLANEMRKILSIYKE-NEL 381
|
330 340 350
....*....|....*....|....*....|..
gi 755605759 379 IAILGMDELSDEDKLVVSRARRIQF---FLSQ 407
Cdd:PRK06793 382 YFKLGTIQENAENAYIFECKNKVEGintFLKQ 413
|
|
| fliI |
PRK07196 |
flagellar protein export ATPase FliI; |
64-408 |
8.13e-40 |
|
flagellar protein export ATPase FliI;
Pssm-ID: 180875 [Multi-domain] Cd Length: 434 Bit Score: 148.50 E-value: 8.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 64 GFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRL-------DPIHREAPDfenlstetEILETGIKV 136
Cdd:PRK07196 74 GVLGGARVFPSEQDGELLIGDSWLGRVINGLGEPLDGKGQLGGSTPLqqqlpqiHPLQRRAVD--------TPLDVGVNA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 137 VDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEP 216
Cdd:PRK07196 146 INGLLTIGKGQRVGLMAGSGVGKSVLLGMITRYTQAD---VVVVGLIGERGREVKEFIEHSLQAAGMAKSVVVAAPADES 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 217 PGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERI-TSTDKGSV 295
Cdd:PRK07196 223 PLMRIKATELCHAIATYYRD-KGHDVLLLVDSLTRYAMAQREIALSLGEPPATKGYPPSAFSIIPRLAESAgNSSGNGTM 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 296 TSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDpEVVGEEHYRVAVEVQQTLQKYREL 375
Cdd:PRK07196 302 TAIYTVLAEGDDQQDPIVDCARAVLDGHIVLSRKLAEAGHYPAIDISQSISRCMS-QVIGSQQAKAASLLKQCYADYMAI 380
|
330 340 350
....*....|....*....|....*....|....*..
gi 755605759 376 QDIIA----ILGMDELSDEdklVVSRARRIQFFLSQN 408
Cdd:PRK07196 381 KPLIPlggyVAGADPMADQ---AVHYYPAITQFLRQE 414
|
|
| PRK05922 |
PRK05922 |
type III secretion system ATPase; Validated |
40-437 |
5.59e-38 |
|
type III secretion system ATPase; Validated
Pssm-ID: 102061 [Multi-domain] Cd Length: 434 Bit Score: 143.51 E-value: 5.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 40 DLTLEValhLGDHSVRTIAMSSTD--GFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAgTRLDPIHREA 117
Cdd:PRK05922 53 PILAEV---IGFHNRTTLLMSLSPihYVALGAEVLPLRRPPSLHLSDHLLGRVLDGFGNPLDGKEQLPK-THLKPLFSSP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 118 PDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDlYYEM 197
Cdd:PRK05922 129 PSPMSRQPIQEIFPTGIKAIDAFLTLGKGQRIGVFSEPGSGKSSLLSTIAKGSKST---INVIALIGERGREVRE-YIEQ 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 198 SDSGVIA-KTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTL 276
Cdd:PRK05922 205 HKEGLAAqRTIIIASPAHETAPTKVIAGRAAMTIAEYFRD-QGHRVLFIMDSLSRWIAALQEVALARGETLSAHHYAASV 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 277 ATEMGRLQERITSTDKGSVTSIQAI-YVP--ADDYTDPAPATTFAHLdATTNLDRKLSEqgiyPAVDPLASTSRALDpEV 353
Cdd:PRK05922 284 FHHVSEFTERAGNNDKGSITALYAIlHYPnhPDIFTDYLKSLLDGHF-FLTPQGKALAS----PPIDILTSLSRSAR-QL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 354 VGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDklvVSRARRIqfflsqnFHVAEQFTGQP-GSYVPVKETVQGF 432
Cdd:PRK05922 358 ALPHHYAAAEELRSLLKAYHEALDIIQLGAYVPGQDAH---LDRAVKL-------LPSIKQFLSQPlSSYCALHNTLKQL 427
|
....*
gi 755605759 433 KEILE 437
Cdd:PRK05922 428 EALLK 432
|
|
| PRK04196 |
PRK04196 |
V-type ATP synthase subunit B; Provisional |
67-410 |
1.57e-33 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 235251 [Multi-domain] Cd Length: 460 Bit Score: 131.49 E-value: 1.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 67 RGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLD-------PIHREAPDfenlstetEILETGIKVVDL 139
Cdd:PRK04196 65 KDTKVRFTGEPLKLPVSEDMLGRIFDGLGRPIDGGPEIIPEKRLDingapinPVAREYPE--------EFIQTGISAIDG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 140 LAPYIKGGKIGLFGGAGVGKtvliQELINNIAQ-------EHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQ 212
Cdd:PRK04196 137 LNTLVRGQKLPIFSGSGLPH----NELAAQIARqakvlgeEENFAVVFAAMGITFEEANFFMEDFEETGALERSVVFLNL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 213 MNEPPGARM---RVAltgLTMAEYFRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQER--I 287
Cdd:PRK04196 213 ADDPAIERIltpRMA---LTAAEYLAFEKGMHVLVILTDMTNYCEALREISAAREEVPGRRGYPGYMYTDLATIYERagR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 288 TSTDKGSVTSIQAIYVPADDYTDPAPattfahlDAT---TN----LDRKLSEQGIYPAVDPLASTSR----ALDPEVVGE 356
Cdd:PRK04196 290 IKGKKGSITQIPILTMPDDDITHPIP-------DLTgyiTEgqivLSRELHRKGIYPPIDVLPSLSRlmkdGIGEGKTRE 362
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 755605759 357 EHYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARRI-QFFLSQNFH 410
Cdd:PRK04196 363 DHKDVANQLYAAYARGKDLRELAAIVGEEALSERDRKYLKFADAFeREFVNQGFD 417
|
|
| ATP-synt_F1_beta_N |
cd18115 |
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of ... |
3-78 |
1.69e-33 |
|
F1-ATP synthase beta (B) subunit, N-terminal domain; The beta (B) subunit of the F1 complex of FoF1-ATP synthase, N-terminal domain. The F-ATP synthase (also called FoF1-ATPase) is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The beta subunit of ATP synthase is catalytic.
Pssm-ID: 349739 [Multi-domain] Cd Length: 76 Bit Score: 120.70 E-value: 1.69e-33
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755605759 3 KGRVTQLMGPVVDVRFEDGQLPAINNALVVRSKQsGEDLTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPI 78
Cdd:cd18115 2 TGKIVQVIGPVVDVEFPEGELPPIYNALEVKGDD-GKKLVLEVQQHLGENTVRAIAMDSTDGLVRGMEVIDTGAPI 76
|
|
| fliI |
PRK07960 |
flagellum-specific ATP synthase FliI; |
65-381 |
3.30e-33 |
|
flagellum-specific ATP synthase FliI;
Pssm-ID: 181182 [Multi-domain] Cd Length: 455 Bit Score: 130.67 E-value: 3.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 65 FQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLDPIhreAPDFENLSTE--TEILETGIKVVDLLAP 142
Cdd:PRK07960 95 YARNISGEGLQSGKQLPLGPALLGRVLDGSGKPLDGLPAPDTGETGALI---TPPFNPLQRTpiEHVLDTGVRAINALLT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 143 YIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMR 222
Cdd:PRK07960 172 VGRGQRMGLFAGSGVGKSVLLGMMARYTQAD---VIVVGLIGERGREVKDFIENILGAEGRARSVVIAAPADVSPLLRMQ 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 223 VALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITS--TDKGSVTSIQA 300
Cdd:PRK07960 249 GAAYATRIAEDFRD-RGQHVLLIMDSLTRYAMAQREIALAIGEPPATKGYPPSVFAKLPALVERAGNgiSGGGSITAFYT 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 301 IYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALdPEVVGEEHYRVAVEVQQTLQKYRELQDIIA 380
Cdd:PRK07960 328 VLTEGDDQQDPIADSARAILDGHIVLSRRLAEAGHYPAIDIEASISRAM-TALIDEQHYARVRQFKQLLSSFQRNRDLVS 406
|
.
gi 755605759 381 I 381
Cdd:PRK07960 407 V 407
|
|
| V_A-ATPase_B |
cd01135 |
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ... |
77-347 |
9.31e-33 |
|
V/A-type ATP synthase subunit B; V/A-type ATP synthase (non-catalytic) subunit B. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria. This subfamily consists of the non-catalytic beta subunit.
Pssm-ID: 410879 [Multi-domain] Cd Length: 282 Bit Score: 125.41 E-value: 9.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 77 PISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLD-------PIHREAPDfenlstetEILETGIKVVDLLAPYIKGGKI 149
Cdd:cd01135 1 VLKLPVSEDMLGRIFNGSGKPIDGGPPILPEDYLDingppinPVARIYPE--------EMIQTGISAIDVMNTLVRGQKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 150 GLFGGAGVGKtvliQELINNIA-------QEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMR 222
Cdd:cd01135 73 PIFSGSGLPH----NELAAQIArqagvvgSEENFAIVFAAMGVTMEEARFFKDDFEETGALERVVLFLNLANDPTIERII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 223 VALTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQER--ITSTDKGSVTSIQA 300
Cdd:cd01135 149 TPRMALTTAEYLAYEKGKHVLVILTDMTNYAEALREVSAAREEVPGRRGYPGYMYTDLATIYERagRVEGRKGSITQIPI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 755605759 301 IYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSR 347
Cdd:cd01135 229 LTMPNDDITHPIPDLTGYITEGQIYLDRDLHNKGIYPPIDVLPSLSR 275
|
|
| PRK04192 |
PRK04192 |
V-type ATP synthase subunit A; Provisional |
103-410 |
1.02e-31 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 235248 [Multi-domain] Cd Length: 586 Bit Score: 127.98 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 103 PLPAGTRLDPihreapdfenlsteTEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAG 182
Cdd:PRK04192 198 PRPYKEKLPP--------------VEPLITGQRVIDTFFPVAKGGTAAIPGPFGSGKTVTQHQLAKWADAD---IVIYVG 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 183 VGERtreGNdlyyEMSD------------SG--------VIAKTAmvfgqmNEPPGARMRVALTGLTMAEYFRDeQGQDV 242
Cdd:PRK04192 261 CGER---GN----EMTEvleefpelidpkTGrplmertvLIANTS------NMPVAAREASIYTGITIAEYYRD-MGYDV 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 243 LLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQER----IT-STDKGSVTSIQAIYVPADDYTDPAPATTF 317
Cdd:PRK04192 327 LLMADSTSRWAEALREISGRLEEMPGEEGYPAYLASRLAEFYERagrvKTlGGEEGSVTIIGAVSPPGGDFSEPVTQNTL 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 318 AHLDATTNLDRKLSEQGIYPAVDPLASTSRALD------PEVVGEEHYRVAVEVQQTLQKYRELQDIIAILGMDELSDED 391
Cdd:PRK04192 407 RIVKVFWALDAELADRRHFPAINWLTSYSLYLDqvapwwEENVDPDWRELRDEAMDLLQREAELQEIVRLVGPDALPEED 486
|
330 340
....*....|....*....|.
gi 755605759 392 KLVVSRARRIQF-FLSQN-FH 410
Cdd:PRK04192 487 RLILEVARLIREdFLQQNaFD 507
|
|
| PRK13343 |
PRK13343 |
F0F1 ATP synthase subunit alpha; Provisional |
45-347 |
2.56e-31 |
|
F0F1 ATP synthase subunit alpha; Provisional
Pssm-ID: 183987 [Multi-domain] Cd Length: 502 Bit Score: 125.80 E-value: 2.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 45 VALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLdPIHREAPDFENLS 124
Cdd:PRK13343 62 FAFNLEEELVGAVLLDDTADILAGTEVRRTGRVLEVPVGDGLLGRVIDPLGRPLDGGGPLQATARR-PLERPAPAIIERD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 125 TETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELInnIAQEHGG-ISVFAGVGERTREGNDLYYEMSDSGVI 203
Cdd:PRK13343 141 FVTEPLQTGIKVVDALIPIGRGQRELIIGDRQTGKTAIAIDAI--INQKDSDvICVYVAIGQKASAVARVIETLREHGAL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 204 AKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRL 283
Cdd:PRK13343 219 EYTTVVVAEASDPPGLQYLAPFAGCAIAEYFRD-QGQDALIVYDDLSKHAAAYRELSLLLRRPPGREAYPGDIFYLHSRL 297
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755605759 284 QERITSTDK----GSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSR 347
Cdd:PRK13343 298 LERAAKLSPelggGSLTALPIIETLAGELSAYIPTNLISITDGQIYLDSDLFAAGQRPAVDVGLSVSR 365
|
|
| V_A-ATPase_A |
cd01134 |
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ... |
112-347 |
1.19e-30 |
|
V/A-type ATP synthase catalytic subunit A; V/A-type ATP synthase catalytic subunit A. These ATPases couple ATP hydrolysis to the build up of a H+ gradient, but V-type ATPases do not catalyze the reverse reaction. Vacuolar (V-type) ATPases play major roles in endomembrane and plasma membrane proton transport in eukaryotes. They are found in multiple intracellular membranes including vacuoles, endosomes, lysosomes, Golgi-derived vesicles, secretory vesicles, as well as the plasma membrane. Archaea have a protein which is similar in sequence to V-ATPases, but functions like an F-ATPase (called A-ATPase). A similar protein is also found in a few bacteria.
Pssm-ID: 410878 [Multi-domain] Cd Length: 288 Bit Score: 119.99 E-value: 1.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 112 PIHREAPDFENLSTeTEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEhggISVFAGVGERtreGN 191
Cdd:cd01134 43 PVRQPRPVKEKLPP-NVPLLTGQRVLDTLFPVAKGGTAAIPGPFGCGKTVISQSLSKWSNSD---VVIYVGCGER---GN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 192 DL------YYEMSD----SGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSA 261
Cdd:cd01134 116 EMaevleeFPELKDpitgESLMERTVLIANTSNMPVAAREASIYTGITIAEYFRD-MGYNVSLMADSTSRWAEALREISG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 262 LLGRMPSAVGYQPTLATEMGRLQER------ITSTDK-GSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQG 334
Cdd:cd01134 195 RLEEMPAEEGYPAYLGARLAEFYERagrvrcLGSPGReGSVTIVGAVSPPGGDFSEPVTQATLRIVQVFWGLDKKLAQRR 274
|
250
....*....|...
gi 755605759 335 IYPAVDPLASTSR 347
Cdd:cd01134 275 HFPSINWLISYSK 287
|
|
| PRK02118 |
PRK02118 |
V-type ATP synthase subunit B; Provisional |
5-316 |
3.95e-25 |
|
V-type ATP synthase subunit B; Provisional
Pssm-ID: 179373 [Multi-domain] Cd Length: 436 Bit Score: 107.04 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 5 RVTQLMGPVVDVRFED---GQLPAINN------ALVVRSKqsGEDLTLEValhlgdhsvrtiaMSSTDGFQRGAEVEDLG 75
Cdd:PRK02118 7 KITDITGNVITVEAEGvgyGELATVERkdgsslAQVIRLD--GDKVTLQV-------------FGGTRGISTGDEVVFLG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 76 RPISVPVGDVTLGRVFNILGEKID-----LDEPLPAGT-RLDPIHREAPdfenlsteTEILETGIKVVDLLAPYIKGGKI 149
Cdd:PRK02118 72 RPMQVTYSESLLGRRFNGSGKPIDggpelEGEPIEIGGpSVNPVKRIVP--------REMIRTGIPMIDVFNTLVESQKI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 150 GLFGGAGVGktvlIQELINNIA-QEHGGISVFAGVGERtregNDLYY----EMSDSGVIAKTAMVFGQMNEPPGARMRVA 224
Cdd:PRK02118 144 PIFSVSGEP----YNALLARIAlQAEADIIILGGMGLT----FDDYLffkdTFENAGALDRTVMFIHTASDPPVECLLVP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 225 LTGLTMAEYFRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQER-ITSTDKGSVTSIQAIYV 303
Cdd:PRK02118 216 DMALAVAEKFALEGKKKVLVLLTDMTNFADALKEISITMDQIPSNRGYPGSLYSDLASRYEKaVDFEDGGSITIIAVTTM 295
|
330
....*....|...
gi 755605759 304 PADDYTDPAPATT 316
Cdd:PRK02118 296 PGDDVTHPVPDNT 308
|
|
| PRK14698 |
PRK14698 |
V-type ATP synthase subunit A; Provisional |
166-402 |
2.28e-22 |
|
V-type ATP synthase subunit A; Provisional
Pssm-ID: 184795 [Multi-domain] Cd Length: 1017 Bit Score: 100.48 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 166 LINNIAQEH-------GGISVFAGVGERTREGNDLYYEM-------SDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMA 231
Cdd:PRK14698 666 LLHNTVTQHqlakwsdAQVVIYIGCGERGNEMTDVLEEFpklkdpkTGKPLMERTVLIANTSNMPVAAREASIYTGITIA 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 232 EYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERI-------TSTDKGSVTSIQAIYVP 304
Cdd:PRK14698 746 EYFRD-MGYDVALMADSTSRWAEALREISGRLEEMPGEEGYPAYLASKLAEFYERAgrvvtlgSDYRVGSVSVIGAVSPP 824
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 305 ADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRALDP------EVVGEEHYRVAVEVQQTLQKYRELQDI 378
Cdd:PRK14698 825 GGDFSEPVVQNTLRVVKVFWALDADLARRRHFPAINWLTSYSLYVDAvkdwwhKNVDPEWKAMRDKAMELLQKEAELQEI 904
|
250 260
....*....|....*....|....
gi 755605759 379 IAILGMDELSDEDKLVVSRARRIQ 402
Cdd:PRK14698 905 VRIVGPDALPERERAILLVARMLR 928
|
|
| V-ATPase_V1_B |
TIGR01040 |
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is ... |
25-393 |
3.72e-22 |
|
V-type (H+)-ATPase V1, B subunit; This models eukaryotic vacuolar (H+)-ATPase that is responsible for acidifying cellular compartments. This enzyme shares extensive sequence similarity with archaeal ATP synthase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273410 [Multi-domain] Cd Length: 466 Bit Score: 98.64 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 25 AINNALVVRSKQSGEDLTLEVALHLGDHSVRTIAMSSTDG-------FQ-------RGAEVEDLGRPISVPVGDVTLGRV 90
Cdd:TIGR01040 7 GVNGPLVILDNVKFPRFAEIVNLTLPDGTVRSGQVLEVSGnkavvqvFEgtsgidaKKTTCEFTGDILRTPVSEDMLGRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 91 FNILGEKIDLDEPLPAGTRLD-------PIHREAPDfenlstetEILETGIKVVDLLAPYIKGGKIGLFGGAGV------ 157
Cdd:TIGR01040 87 FNGSGKPIDKGPPVLAEDYLDingqpinPYARIYPE--------EMIQTGISAIDVMNSIARGQKIPIFSAAGLphneia 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 158 -------GKTVLIQELINNIAQEHGGIsVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTM 230
Cdd:TIGR01040 159 aqicrqaGLVKLPTKDVHDGHEDNFAI-VFAAMGVNMETARFFKQDFEENGSMERVCLFLNLANDPTIERIITPRLALTT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 231 AEYFRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTD--KGSVTSIQAIYVPADDY 308
Cdd:TIGR01040 238 AEYLAYQCEKHVLVILTDMSSYADALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEgrNGSITQIPILTMPNDDI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 309 TDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRaLDPEVVGE-----EHYRVAVEVQQTLQKYRELQDIIAILG 383
Cdd:TIGR01040 318 THPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSR-LMKSAIGEgmtrkDHSDVSNQLYACYAIGKDVQAMKAVVG 396
|
410
....*....|
gi 755605759 384 MDELSDEDKL 393
Cdd:TIGR01040 397 EEALSSEDLL 406
|
|
| F1-ATPase_alpha_CD |
cd01132 |
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma ... |
78-347 |
5.60e-22 |
|
F1 ATP synthase alpha subunit, central domain; The F-ATPase is found in bacterial plasma membranes, mitochondrial inner membranes and in chloroplast thylakoid membranes. It has also been found in the archaea Methanosarcina barkeri. It uses a proton gradient to drive ATP synthesis and hydrolyzes ATP to build the proton gradient. The mitochondrial extrinsic membrane domain, F1, is composed of alpha, beta, gamma, delta and epsilon subunits with a stoichiometry of 3:3:1:1:1. The alpha subunit of the F1 ATP synthase can bind nucleotides, but is non-catalytic. Alpha and beta subunits form the globular catalytic moiety, a hexameric ring of alternating alpha and beta subunits. Gamma, delta and epsilon subunits form a stalk, connecting F1 to F0, the integral membrane proton-translocating domain.
Pssm-ID: 410876 [Multi-domain] Cd Length: 274 Bit Score: 95.32 E-value: 5.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 78 ISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRlDPIHREAPDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGV 157
Cdd:cd01132 2 VEVPVGEALLGRVVDALGNPIDGKGPIQTKER-RRVESKAPGIIPRQSVNEPLQTGIKAIDSLIPIGRGQRELIIGDRQT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 158 GKT-VLIQELINNiaQEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRD 236
Cdd:cd01132 81 GKTaIAIDTIINQ--KGKKVYCIYVAIGQKRSTVAQIVKTLEEHGAMEYTIVVAATASDPAPLQYLAPYAGCAMGEYFRD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 237 eQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLATEMGRLQERITSTDK----GSVTSIQAIYVPADDYTDPA 312
Cdd:cd01132 159 -NGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSDelggGSLTALPIIETQAGDVSAYI 237
|
250 260 270
....*....|....*....|....*....|....*
gi 755605759 313 PATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSR 347
Cdd:cd01132 238 PTNVISITDGQIFLESELFNKGIRPAINVGLSVSR 272
|
|
| PTZ00185 |
PTZ00185 |
ATPase alpha subunit; Provisional |
51-375 |
3.44e-17 |
|
ATPase alpha subunit; Provisional
Pssm-ID: 140212 [Multi-domain] Cd Length: 574 Bit Score: 83.94 E-value: 3.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 51 DHSVRTIAMSSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLD------EPLPAGTRLDPIHREAPDFENLS 124
Cdd:PTZ00185 88 DGRIGIILMDNITEVQSGQKVMATGKLLYIPVGAGVLGKVVNPLGHEVPVGlltrsrALLESEQTLGKVDAGAPNIVSRS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 125 TETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT-VLIQELINN------IAQEHGGISVFAGVGERTREGNDLYYEM 197
Cdd:PTZ00185 168 PVNYNLLTGFKAVDTMIPIGRGQRELIVGDRQTGKTsIAVSTIINQvrinqqILSKNAVISIYVSIGQRCSNVARIHRLL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 198 SDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTLA 277
Cdd:PTZ00185 248 RSYGALRYTTVMAATAAEPAGLQYLAPYSGVTMGEYFMN-RGRHCLCVYDDLSKQAVAYRQISLLLRRPPGREAYPGDVF 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 278 TEMGRLQER--ITSTDK--GSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSRaLDPEV 353
Cdd:PTZ00185 327 YLHSRLLERaaMLSPGKggGSVTALPIVETLSNDVTAYIVTNVISITDGQIYLDTKLFTGGQRPAVNIGLSVSR-VGSSA 405
|
330 340
....*....|....*....|..
gi 755605759 354 VGEEHYRVAVEVQQTLQKYREL 375
Cdd:PTZ00185 406 QNVAMKAVAGKLKGILAEYRKL 427
|
|
| ATP-synt_ab_N |
pfam02874 |
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase ... |
6-75 |
5.37e-17 |
|
ATP synthase alpha/beta family, beta-barrel domain; This family includes the ATP synthase alpha and beta subunits the ATP synthase associated with flagella.
Pssm-ID: 427029 [Multi-domain] Cd Length: 69 Bit Score: 75.27 E-value: 5.37e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 6 VTQLMGPVVDVRFEDGQLPAINNALVVRsKQSGEDLTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLG 75
Cdd:pfam02874 1 IVQVIGPVVDVEFGIGRLPGLLNALEVE-LVEFGSLVLGEVLNLGGDKVRVQVFGGTSGLSRGDEVKRTG 69
|
|
| AtpA |
COG0056 |
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP ... |
36-267 |
5.76e-17 |
|
FoF1-type ATP synthase, alpha subunit [Energy production and conversion]; FoF1-type ATP synthase, alpha subunit is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 439826 [Multi-domain] Cd Length: 504 Bit Score: 83.16 E-value: 5.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 36 QSGEDLTLE-----VALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRL 110
Cdd:COG0056 48 MAGELLEFPggvygMALNLEEDNVGVVLLGDYEGIKEGDTVKRTGRILSVPVGEALLGRVVDPLGRPIDGKGPIEAEERR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 111 dPIHREAPDFENLSTETEILETGIKVVDLLAPyikggkIG------LFGGAGVGKT-VLIQELINniaQEHGGI------ 177
Cdd:COG0056 128 -PVERPAPGVIDRQPVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTaIAIDTIIN---QKGKDViciyva 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 178 -----SVFAGVGERTREGNDLYYemsdSGVIAKTAmvfgqmNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRF 252
Cdd:COG0056 198 igqkaSTVAQVVETLEEHGAMEY----TIVVAATA------SDPAPLQYIAPYAGCAMGEYFMD-QGKDVLIVYDDLSKH 266
|
250
....*....|....*
gi 755605759 253 TQAGMEVSALLGRMP 267
Cdd:COG0056 267 AVAYRELSLLLRRPP 281
|
|
| ATP-synt_F1_V1_A1_AB_FliI_C |
cd01429 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
358-427 |
3.24e-16 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, C-terminal domain; The alpha and beta (also called A and B) subunits are primarily found in the F1, V1, and A1 complexes of F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex that forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349744 [Multi-domain] Cd Length: 70 Bit Score: 72.86 E-value: 3.24e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 358 HYRVAVEVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARRIQFFLSQNFHVAEQFTGQPGSYVPVKE 427
Cdd:cd01429 1 HKAVARGFKAILAQYRELRDIVAIVGDDALSEADKKTLSRGRRLEEFLQQGQFEPETIEDTLEKLYPIKE 70
|
|
| PRK09281 |
PRK09281 |
F0F1 ATP synthase subunit alpha; Validated |
42-267 |
1.47e-15 |
|
F0F1 ATP synthase subunit alpha; Validated
Pssm-ID: 236448 [Multi-domain] Cd Length: 502 Bit Score: 78.57 E-value: 1.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 42 TLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPAGTRLdPIHREAPDFE 121
Cdd:PRK09281 59 VYGIALNLEEDNVGAVILGDYEDIKEGDTVKRTGRILEVPVGEALLGRVVNPLGQPIDGKGPIEATETR-PVERKAPGVI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 122 NLSTETEILETGIKVVDLLAPyikggkIG------LFGGAGVGKT-VLIQELINniaQEHGGI-----------SVFAGV 183
Cdd:PRK09281 138 DRKSVHEPLQTGIKAIDAMIP------IGrgqrelIIGDRQTGKTaIAIDTIIN---QKGKDViciyvaigqkaSTVAQV 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 184 GERTREGNDLYYemsdSGVIAKTAmvfgqmNEPPGARMRVALTGLTMAEYFRDeQGQDVLLFIDNIFRFTQAGMEVSALL 263
Cdd:PRK09281 209 VRKLEEHGAMEY----TIVVAATA------SDPAPLQYLAPYAGCAMGEYFMD-NGKDALIVYDDLSKQAVAYRQLSLLL 277
|
....
gi 755605759 264 GRMP 267
Cdd:PRK09281 278 RRPP 281
|
|
| atpA |
CHL00059 |
ATP synthase CF1 alpha subunit |
39-347 |
6.48e-14 |
|
ATP synthase CF1 alpha subunit
Pssm-ID: 176999 [Multi-domain] Cd Length: 485 Bit Score: 73.46 E-value: 6.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 39 EDLTLEVALHLGDHSVRTIAMSSTDGFQRGAEVEDLGRPISVPVGDVTLGRVFNILGEKIDLDEPLPA-GTRLdpIHREA 117
Cdd:CHL00059 35 EDGTIGIALNLESNNVGVVLMGDGLMIQEGSSVKATGKIAQIPVSEAYLGRVVNALAKPIDGKGEISAsESRL--IESPA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 118 PDFENLSTETEILETGIKVVDLLAPYIKGGKIGLFGGAGVGKT-VLIQELINNIAQehGGISVFAGVGERTREGNDLYYE 196
Cdd:CHL00059 113 PGIISRRSVYEPLQTGLIAIDSMIPIGRGQRELIIGDRQTGKTaVATDTILNQKGQ--NVICVYVAIGQKASSVAQVVTT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 197 MSDSGVIAKTAMVFGQMNEPPGARMRVALTGLTMAEYFRdEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAVGYQPTL 276
Cdd:CHL00059 191 LQERGAMEYTIVVAETADSPATLQYLAPYTGAALAEYFM-YRGRHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAYPGDV 269
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755605759 277 ATEMGRLQERIT-STDK---GSVTSIQAIYVPADDYTDPAPATTFAHLDATTNLDRKLSEQGIYPAVDPLASTSR 347
Cdd:CHL00059 270 FYLHSRLLERAAkLSSQlgeGSMTALPIVETQAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR 344
|
|
| PRK12608 |
PRK12608 |
transcription termination factor Rho; Provisional |
64-347 |
1.94e-10 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237150 [Multi-domain] Cd Length: 380 Bit Score: 62.41 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 64 GFQRGAEVEDLGRPISvpvGDVTLGRVFNILGEKIDLDEPLPAGTRLDPIHreaPDfENLSTETEILETGIKVVDLLAPY 143
Cdd:PRK12608 58 NLRTGDVVEGVARPRE---RYRVLVRVDSVNGTDPEKLARRPHFDDLTPLH---PR-ERLRLETGSDDLSMRVVDLVAPI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 144 IKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VGERTREGNDLYYEMSdsgviaktAMVFGQMNEPPGARmR 222
Cdd:PRK12608 131 GKGQRGLIVAPPRAGKTVLLQQIAAAVAANHPEVHLMVLlIDERPEEVTDMRRSVK--------GEVYASTFDRPPDE-H 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 223 VALTGLTMAEYFRD-EQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSavGYQPTLATEMGRlqeRITSTDK-----GSVT 296
Cdd:PRK12608 202 IRVAELVLERAKRLvEQGKDVVILLDSLTRLARAYNNEVESSGRTLS--GGVDARALQRPK---RLFGAARnieegGSLT 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755605759 297 SIQAIYVP----ADDYtdpapatTFAHLDATTN----LDRKLSEQGIYPAVDPLASTSR 347
Cdd:PRK12608 277 IIATALVDtgsrMDEV-------IFEEFKGTGNmeivLDRELADKRVFPAIDIAKSGTR 328
|
|
| rho |
TIGR00767 |
transcription termination factor Rho; This RNA helicase, the transcription termination factor ... |
96-408 |
2.43e-10 |
|
transcription termination factor Rho; This RNA helicase, the transcription termination factor Rho, occurs in nearly all bacteria but is missing from the Cyanobacteria, the Mollicutes (Mycoplasmas), and various Lactobacillales including Streptococcus. It is also missing, of course, from the Archaea, which also lack Nus factors. Members of this family from Micrococcus luteus, Mycobacterium tuberculosis, and related species have a related but highly variable long, highly charged insert near the amino end. Members of this family differ in the specificity of RNA binding. [Transcription, Transcription factors]
Pssm-ID: 162030 [Multi-domain] Cd Length: 415 Bit Score: 62.01 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 96 EKIDLDEPLPAGTR-----LDPIHreaPDFE-NLSTETEILETgiKVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINN 169
Cdd:TIGR00767 117 ESVNGDDPEKAKNRvlfenLTPLY---PNERlRLETSTEDLST--RVLDLFAPIGKGQRGLIVAPPKAGKTVLLQKIAQA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 170 IAQEHGGISVFAG-VGERTREGNDLyyEMSDSG-VIAKTamvfgqMNEPPGARMRVALTGLTMAEYfRDEQGQDVLLFID 247
Cdd:TIGR00767 192 ITRNHPEVELIVLlIDERPEEVTDM--QRSVKGeVVAST------FDEPASRHVQVAEMVIEKAKR-LVEHKKDVVILLD 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 248 NIFRFTQAGMEVSALLGRM------PSAVgYQPTLATEMGRLQEritstDKGSVTSIQAIYVPADDYTDpapATTFAHLD 321
Cdd:TIGR00767 263 SITRLARAYNTVTPASGKVlsggvdANAL-HRPKRFFGAARNIE-----EGGSLTIIATALIDTGSRMD---EVIFEEFK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 322 ATTN----LDRKLSEQGIYPAVDPLASTSRAlDPEVVGEEHyrvavevqqtLQKYRELQDIIAilGMDElSDEDKLVVSR 397
Cdd:TIGR00767 334 GTGNmelhLDRKLADRRIFPAIDIKKSGTRK-EELLLTPEE----------LQKIWVLRKIIS--PMDS-IEAMEFLISK 399
|
330
....*....|....*
gi 755605759 398 ARRI----QFFLSQN 408
Cdd:TIGR00767 400 LKKTktneEFLESMK 414
|
|
| ATP-synt_F1_V1_A1_AB_FliI_N |
cd01426 |
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, ... |
3-76 |
6.91e-09 |
|
ATP synthase, alpha/beta subunits of F1/V1/A1 complex, flagellum-specific ATPase FliI, N-terminal domain; The alpha and beta (or A and B) subunits are primarily found in the F1, V1, and A1 complexes of the F-, V- and A-type family of ATPases with rotary motors. These ion-transporting rotary ATPases are composed of two linked multi-subunit complexes: the F1, V1, or A1 complex which contains three copies each of the alpha and beta subunits that form the soluble catalytic core involved in ATP synthesis/hydrolysis, and the Fo, Vo, or Ao complex which forms the membrane-embedded proton pore. The F-ATP synthases (also called FoF1-ATPases) are found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts, or in the plasma membranes of bacteria. F-ATPases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. The A-ATP synthases (AoA1-ATPases), a different class of proton-translocating ATP synthases, are found in archaea and function like F-ATP synthases. Structurally, however, the A-ATP synthases are more closely related to the V-ATP synthases (vacuolar VoV1-ATPases), which are a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, F-, V-, and A-type synthases can function in both ATP synthesis and hydrolysis modes. This family also includes the flagellum-specific ATPase/type III secretory pathway virulence-related protein, which shows extensive similarity to the alpha and beta subunits of F1-ATP synthase.
Pssm-ID: 349738 [Multi-domain] Cd Length: 73 Bit Score: 52.31 E-value: 6.91e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755605759 3 KGRVTQLMGPVVDVRFEDGqlPAINNALVVRSK--QSGEDLTLEVALHLGDhSVRTIAMSSTDGFQRGAEVEDLGR 76
Cdd:cd01426 1 KGRVIRVNGPLVEAELEGE--VAIGEVCEIERGdgNNETVLKAEVIGFRGD-RAILQLFESTRGLSRGALVEPTGR 73
|
|
| rho_factor_C |
cd01128 |
C-terminal ATP binding domain of transcription termination factor rho; Transcription ... |
135-347 |
2.33e-08 |
|
C-terminal ATP binding domain of transcription termination factor rho; Transcription termination factor rho is a bacterial ATP-dependent RNA/DNA helicase. It is a homohexamer. Each monomer consists of an N-terminal oligonucleotide/oligosaccharide binding fold (OB-fold) domain which binds cysteine-rich nucleotides, and a C-terminal ATP binding domain. This alignment is of the C-terminal ATP binding domain.
Pssm-ID: 410872 [Multi-domain] Cd Length: 249 Bit Score: 54.90 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 135 KVVDLLAPYIKGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAG-VGERTREGNDlyyeMSDSG---VIAKTamvf 210
Cdd:cd01128 5 RVIDLIAPIGKGQRGLIVAPPKAGKTTLLQNIANAIAKNHPEVELIVLlIDERPEEVTD----MRRSVkgeVVAST---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 211 gqMNEPPGARMRVALTGLTMAEYfRDEQGQDVLLFIDNIFRFTQAGMEVSALLGRMPSAvGYQPTlATEMGRlqeRITST 290
Cdd:cd01128 77 --FDEPPERHVQVAEMVIEKAKR-LVEHGKDVVILLDSITRLARAYNTVVPSSGKTLSG-GVDAN-ALHKPK---RFFGA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755605759 291 -----DKGSVTSIQAIYVPADDYTDPApatTFAHLDATTN----LDRKLSEQGIYPAVDPLASTSR 347
Cdd:cd01128 149 arnieEGGSLTIIATALVDTGSRMDEV---IFEEFKGTGNmelvLDRKLAEKRIFPAIDILKSGTR 211
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
145-266 |
2.31e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 47.37 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 145 KGGKIGLFGGAGVGKTVLIQELINNIAQEHGGISVFAGVGERTREGNDLYYEMSDSGVIAKTamvfgqmnepPGARMRVA 224
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGS----------GELRLRLA 70
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 755605759 225 ltgLTMAEYFRDEqgqdvLLFIDNIFRFTQAGMEVSALLGRM 266
Cdd:smart00382 71 ---LALARKLKPD-----VLILDEITSLLDAEQEALLLLLEE 104
|
|
| ATP-synt_V_A-type_alpha_C |
cd18111 |
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of ... |
364-416 |
1.68e-05 |
|
V/A-type ATP synthase catalytic subunit A (alpha), C-terminal domain; The alpha (A) subunit of the V1/A1 complex of V/A-type ATP synthases, C-terminal domain. The V- and A-type family of ATPases are composed of two linked multi-subunit complexes: the V1 and A1 complexes contain three copies each of the alpha and beta subunits that form the soluble catalytic core, which is involved in ATP synthesis/hydrolysis, and the Vo or Ao complex that forms the membrane-embedded proton pore. The A-ATP synthase (AoA1-ATPase) is found in archaea and functions like F-ATP synthase. Structurally, however, the A-ATP synthase is more closely related to the V-ATP synthase (vacuolar VoV1-ATPase), which is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. Collectively, the V- and A-type synthases can function in both ATP synthesis and hydrolysis modes.
Pssm-ID: 349746 [Multi-domain] Cd Length: 105 Bit Score: 43.53 E-value: 1.68e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 755605759 364 EVQQTLQKYRELQDIIAILGMDELSDEDKLVVSRARRI-QFFLSQN-FHVAEQFT 416
Cdd:cd18111 7 EAMEILQEEAELQEIVQLVGPDALPEEDRLTLEVARMIrEDFLQQNaFDEVDTYC 61
|
|
| rho |
PRK09376 |
transcription termination factor Rho; Provisional |
115-347 |
1.74e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 236490 [Multi-domain] Cd Length: 416 Bit Score: 47.06 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 115 REAPDFENLS----TETEILETGI------KVVDLLAPYIKG--GKIglfggagV-----GKTVLIQELINNIAQEHGGI 177
Cdd:PRK09376 128 RNRPLFENLTplypNERLRLETGNpedlstRIIDLIAPIGKGqrGLI-------VappkaGKTVLLQNIANSITTNHPEV 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 178 SVFAG-VGERTREGNDlyyeMSDS---GVIAKTamvfgqMNEPPGARMRVALTGLTMAEyfRD-EQGQDVLLFIDNIFRF 252
Cdd:PRK09376 201 HLIVLlIDERPEEVTD----MQRSvkgEVVAST------FDEPAERHVQVAEMVIEKAK--RLvEHGKDVVILLDSITRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755605759 253 TQA--------------GMEVSALlgrmpsavgYQPT------LATEMGrlqeritstdkGSVTSIqaiyvpaddytdpa 312
Cdd:PRK09376 269 ARAyntvvpssgkvlsgGVDANAL---------HRPKrffgaaRNIEEG-----------GSLTII-------------- 314
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 755605759 313 pATT------------FAHLDATTN----LDRKLSEQGIYPAVDPLASTSR 347
Cdd:PRK09376 315 -ATAlidtgsrmdeviFEEFKGTGNmelhLDRKLAEKRIFPAIDINRSGTR 364
|
|
| |
